Research Article

Biochemical and Pharmacological Characterization of TLBbar, a New Serine Protease with Coagulant Activity from Bothrops barnetti Snake Venom

Figure 4

Kinetic properties and inhibition of the thrombin-like enzyme TLBbar from B. barnetti venom upon BApNA substrate. (a) Proteolytic activity of the whole venom B. barnetti (WV) Bbt Ia and TLBbar fractions. (b) Inhibition of the proteolytic activity of TLBbar by PMSF (phenylmethyl sulfonyl fluoride), Leupeptin (acetyl-leucyl-leucyl-argial) EGTA (acid glycol-bis (2 aminoetileter)-N,N,N,N-tetracetic), EDTA (Ethylenediamine tetraacetic acid), SBT-I (Soybean trypsin inhibitor), and heparin. (c) Effect of substrate concentration. (d) Lineweaver-Burk (double-reciprocal) plot. (e) Effect of temperature. (f) Effect of pH. The results of all experiments are the . of three determinations ( ).
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